Frozen assembly of gold nanoparticles for rapid analysis of antifreeze protein activity
- Authors
- Park, Ji-In; Lee, Jun Hyuck; Gwak, Yunho; Kim, Hak Jun; Jin, EonSeon; Kim, Young-Pil
- Issue Date
- Mar-2013
- Publisher
- ELSEVIER ADVANCED TECHNOLOGY
- Keywords
- Gold nanoparticle; Frozen assembly; Antifreeze protein; Ice-binding protein; Thermal hysteresis
- Citation
- BIOSENSORS & BIOELECTRONICS, v.41, pp.752 - 757
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOSENSORS & BIOELECTRONICS
- Volume
- 41
- Start Page
- 752
- End Page
- 757
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/163321
- DOI
- 10.1016/j.bios.2012.09.052
- ISSN
- 0956-5663
- Abstract
- We report the novel activity-based detection of antifreeze protein (APP), also known as ice-binding protein (IBP), using freeze-labile gold nanoparticles (AuNPs) in order to overcome labor-intensive and low throughput issues of the current method based on thermal hysteresis (TH). Upon the addition of either CnAFP from the Antarctic diatom Chaetoceros neogracile or LeIBP from the Arctic yeast Leucosporidium sp. to mercaptosuccinic acid-capped AuNP, the self-assembly of AuNPs was highly inhibited after a freezing/thawing cycle, leading to no color change in the AuNP solution. As a result, the aggregation parameter (E-520/E-650) of AuNP presented the rapid detection of both the concentration-dependent activity and stability of two AFPs with high sensitivity, where the detection range was 100-fold lower than that of the TH-based method. We suggest that our newly developed method is very suitable for simple and high-throughput measurement of AFP activity.
- Files in This Item
-
Go to Link
- Appears in
Collections - 서울 자연과학대학 > 서울 생명과학과 > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/163321)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.